3aj4
From Proteopedia
Crystal structure of the PH domain of Evectin-2 from human complexed with O-phospho-L-serine
Structural highlights
Function[PKHB2_HUMAN] Involved in retrograde transport of recycling endosomes.[1] [2] Publication Abstract from PubMedPhosphatidylserine (PS) is a relatively minor constituent of biological membranes. Despite its low abundance, PS in the plasma membrane (PM) plays key roles in various phenomena such as the coagulation cascade, clearance of apoptotic cells, and recruitment of signaling molecules. PS also localizes in endocytic organelles, but how this relates to its cellular functions remains unknown. Here we report that PS is essential for retrograde membrane traffic at recycling endosomes (REs). PS was most concentrated in REs among intracellular organelles, and evectin-2 (evt-2), a protein of previously unknown function, was targeted to REs by the binding of its pleckstrin homology (PH) domain to PS. X-ray analysis supported the specificity of the binding of PS to the PH domain. Depletion of evt-2 or masking of intracellular PS suppressed membrane traffic from REs to the Golgi. These findings uncover the molecular basis that controls the RE-to-Golgi transport and identify a unique PH domain that specifically recognizes PS but not polyphosphoinositides. Intracellular phosphatidylserine is essential for retrograde membrane traffic through endosomes.,Uchida Y, Hasegawa J, Chinnapen D, Inoue T, Okazaki S, Kato R, Wakatsuki S, Misaki R, Koike M, Uchiyama Y, Iemura S, Natsume T, Kuwahara R, Nakagawa T, Nishikawa K, Mukai K, Miyoshi E, Taniguchi N, Sheff D, Lencer WI, Taguchi T, Arai H Proc Natl Acad Sci U S A. 2011 Sep 20;108(38):15846-51. Epub 2011 Sep 12. PMID:21911378[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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